Human Galectin-9 Antibody Summary
Met1-Thr323
Accession # NP_002299
Applications
This antibody functions as an ELISA capture antibody when paired with Mouse Anti-Human Galectin‑9 Monoclonal Antibody (Catalog # MAB20452).
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human Galectin-9 DuoSet ELISA Kit (Catalog # DY2045) for convenient development of a sandwich ELISA or the Human Galectin-9 Quantikine ELISA Kit (Catalog # DGAL90) for a complete optimized ELISA.
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Human Galectin‑9 ELISA Standard Curve. Recombinant Human Galectin-9 protein was serially diluted 2-fold and captured by Mouse Anti-Human Galectin-9 Monoclonal Antibody (Catalog # MAB20451) coated on a Clear Polystyrene Microplate (Catalog # DY990). Mouse Anti-Human Galectin-9 Monoclonal Antibody (Catalog # MAB20452) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Galectin-9
Galectins comprise a family of multifunctional carbohydrate-binding proteins with specificity for N‑acetyl-lactosamine-containing glycoproteins. At least 14 mammalian Galectins share structural similarities in their carbohydrate recognition domains (CRD), forming three groups: prototype (one CRD), tandem-repeat (two CRDs), and chimeric (one CRD, unique N‑terminus) (1, 2). Full length Galectin-9 is a widely expressed 39 kDa tandem-repeat Galectin that contains two CRDs connected by a linker region (3). Progressive deletion within the linker region generates a 36 kDa isoform, also known as Ecalectin or UAT, as well as a 35 kDa isoform (4). This recombinant protein corresponds to the Ecalectin isoform of human Galectin-9 and shares 70% and 73% aa sequence identity with the corresponding regions of mouse and rat Galectin-9, respectively. Galectin-9 exhibits a wide range of activities. All three isoforms function as eosinophil chemoattractants (5, 6). This activity is destroyed by thrombin-mediated cleavage within the linker region of the long isoform, although the Ecalectin isoform is resistant to thrombin (7). Galectin-9 binds to carbohydrate moieties of IgE, thereby preventing immune complex formation, mast cell degranulation, and asthmatic and cutaneous anaphylaxis reactions (8). Independent of its lectin properties, Galectin-9 induces the maturation of dendritic cells which promote Th1 polarization (9). Galectin-9 induces cellular apoptosis in part by direct binding to TIM-3 (10, 11). Its interaction with TIM-3 inhibits Th1 cell and CD8+ cytotoxic T cell responses and also promotes regulatory T cell differentiation and activity (11, 12). Galectin-9 suppresses tumor cell metastasis by interfering with the associations between hyaluronic acid and CD44 and between VCAM-1 and Integrin alpha 4 beta 1 (13). The Ecalectin isoform (UAT; urate transporter) can also be expressed as an integral membrane protein and mediate the cellular efflux of urate (14).
- Yang, R-Y. et al. (2008) Expert Rev. Mol. Med. 10:e17.
- Elola, M. T. et al. (2007) Cell. Mol. Life Sci. 64:1679.
- Tureci, O. et al. (1997) J. Biol. Chem. 272:6416.
- Chabot, S. et al. (2002) Glycobiology 12:111.
- Matsumoto, R. et al. (2002) J. Immunol. 168:1961.
- Sato, M. et al. (2002) Glycobiology 12:191.
- Nishi, N. et al. (2006) Glycobiology 16:15C.
- Niki, T. et al. (2009) J. Biol. Chem. 284:32344.
- Dai, S.-Y. et al. (2005) J. Immunol. 175:2974.
- Seki, M. et al. (2007) Arthritis Rheum. 56:3968.
- Zhu, C. et al. (2005) Nat. Immunol. 6:1245.
- Sehrawat, S. et al. (2010) PloS Pathogens 6:e1000882.
- Nobumoto, A. et al. (2008) Glycobiology 18:735.
- Leal-Pinto, E. et al. (2002) Am. J. Physiol. Renal Physiol. 283:F150.
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